ID G8YGA4_PICSO Unreviewed; 1564 AA.
AC G8YGA4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Helicase SWR1 {ECO:0000256|ARBA:ARBA00040599};
GN Name=Piso0_003573 {ECO:0000313|EMBL:CCE81221.1};
GN ORFNames=GNLVRS01_PISO0G15296g {ECO:0000313|EMBL:CCE80456.1},
GN GNLVRS01_PISO0H15297g {ECO:0000313|EMBL:CCE81221.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE81221.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|EMBL:CCE81221.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- FUNCTION: Catalytic component of the SWR1 complex which mediates the
CC ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading
CC to transcriptional regulation of selected genes by chromatin
CC remodeling. {ECO:0000256|ARBA:ARBA00037570}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO082053; CCE80456.1; -; Genomic_DNA.
DR EMBL; FO082052; CCE81221.1; -; Genomic_DNA.
DR STRING; 559304.G8YGA4; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; G8YGA4; -.
DR OMA; CENNDKE; -.
DR Proteomes; UP000005222; Chromosome G.
DR Proteomes; UP000005222; Chromosome H.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 374..446
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 750..915
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1292..1442
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..630
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1564 AA; 178972 MW; 6F8ACA6C384B4E05 CRC64;
MPVNKGRRKG KSRTENNVSV KKETKPKPSL LPQKRKLNGT NSGAKSQQSH QNKKVRFANE
LSQEQNRLAE IIAEFNITLS ELFQLKEYKS LVFWEPKEFL ASLHSNSVPE IIDYFLNNTG
YRLSWMKDAK DLSDIPLRLQ KKALHDQEIK IKEKYPFRDE VMNRSREIEL DLLSNIEVAP
EPEKPISKRK QVSVKSEPAA ITPNIKSDDS LHEHYEVINQ NLKINRVKFS INAPIITHPS
HIPSWRSEQN DSIKASKDEK ITDYIPKSLE VIASKDNTEI VPNVGNQIRH FLETRYKSPI
IDETSTTDYK FTLEEYEKVM DQQINLFKKL NEKIYLKKSL ELNGDKIEKR KTVLPHSSNS
KQQVDLFRQY SYLKPQLAGV QSSSTYLDNF LHQAVVFSKT HQNVRKNHQL RARKIAQMIE
QHFKKKRGEK ERLARDREQN LKRLSKIAVS AVKKRWTQAL KVYRYLQQEK EEELRKIKGR
EHLSQMLEHS TQLLEAQLNR KSKDDSNSDT GDDYSITPLP EDPDMKSHDS SKFTSSESGT
SESSDTENSD SEAGTLSALY DGTEIDQDKL DVESYMDYSE KEKAIIEESS KNVPDSFLDS
DSSSDELDSD DDSDEDNEES TDDMDGDINE NSQSEDTSGV KNSENGEGST LSLLGNDNID
DESDDMSVKF NSSEDSIESD NMSSSDNEME DEPKTPRSSE SSDRMGDRKN SSNIELEDEV
NGSKVRDVPI PSLLRGTLRP YQKQGLNWLA SLYNNNTNGI LADEMGLGKT IQTISLLAYL
ACEHGIWGPH LIIVPTSVML NWEMEFKKFA PGFKVLTYYG SPQQRAQKRK GWNKPDTFHV
CITSYQLVVH DHQSFKRRKW RYMILDEAHN IKNFRSARWR ALLNFNTENR LLLTGTPLQN
NLIELWSLLY FLMPSSKVNQ AMPDGFANLD DFQNWFGRPV DRILEQSTSG GNAELSNLGD
TAMDNMDEET KNTVARLHQV LRPYLLRRLK RDVETQMPAK YEHVVYCRLS KRQRFLYDEF
MSRAQTKETL ASGNFLSIIN CLMQLRKVCN HPDLFEVRPI LTSFVIPRSV SGRVKDSLGF
VQNRLLVDDK RNDVSFSNLN LDVTNHDMLD YFVSSSINKL QSTAEIESQI AQLDKLIALS
EEYKSSNSDN VLNYYRSMKL KRQIDTREKF IHLLYLNKLR CGRMPLMGGK LISFLKCLKK
VTCTSVYDEA VNSIAQQAAN AESMIEKFSV ITPSVVALDM VDQLVPISTQ KLIRSEVFQG
KIENPFHKSQ VKLSIAFPDK SLLQYDCGKL QKLAQLMQQL TSEGHRALIF TQMTKVLDIL
EQFLNIHGYR YMRLDGATKI EDRQLLTEKF NRDPKIPVFI LSTRSGGLGI NLTGADTVIF
YDSDWNPAMD KQCQDRCHRI GQSRDVHIYR FVSEYTIESN ILRKANQKRQ LDNVVIQEGE
FTTDYFGKFS VKDLVNDVSG GNEAVKENIE SSDTGNMESV LAQVEDEDDR AAAQEAMKEA
AIDEEDFDDT NKPGSSSATP AAPDNQTPNA EPAGSKGDDL DYEDGVGHID EYMLRFIANG
YYWD
//
